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USP15生物学功能的研究进展 被引量:1

Research Progress in Tumor and Immune Mechanism of USP15
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摘要 去泛素化酶(DUBs)是体内分解蛋白泛素链的一类蛋白酶体系,对蛋白泛素化降解过程起校正作用。泛素特异性蛋白酶(USP)家族是DUBs中最大的家族,通过多种途径参与免疫应答,且与一些疾病和肿瘤的发生具有明显相关性。USP15是USP家族的重要组成部分,参与调节转化生长因子β、p53、核因子κB等重要的信号转导通路,与一些肿瘤的发生发展相关。USP15也可通过调节I型干扰素产生和T细胞活化参与免疫反应,并具有多种重要生物学功能,包括维持基因稳定性、调节转录因子及抗病毒等重要的细胞活动。 Deubiquitinases(DUBs) are a class of enzyme protein systems that decompose protein ubiquitin chains in vivo,correcting the process of protein ubiquitination and degradation.The ubiquitin-specific protease(USP) family is the largest family in DUBs,which is involved in the immune response through a variety of pathways and has a significant correlation with the occurrence of some diseases and tumors.USP15 is an important component of the USP family,participating in regulating important signal transduction pathways of transforming growth factor-β,p53 and nuclear factor-κ B,associated with the development of some tumors.USP15 also participates in immune responses by regulating type I interferon production and T cell activation,and has a variety of important biological functions,including maintaining gene stability,regulating transcription factors,and antiviral activity,and other important cellular activities.
作者 谢敏 李万颖 洪晓玲 王淑华 张松灵 XIE Min;LI Wanying;HONG Xiaoling;WANG Shuhua;ZHANG Songling(Department of Tumor Gynecology,Jilin University First Hospital,Changchun 130021,China)
出处 《医学综述》 2019年第7期1282-1286,共5页 Medical Recapitulate
基金 吉林省科技发展计划白求恩专项(20160101049JC)
关键词 去泛素化酶 泛素特异性蛋白酶15 肿瘤 免疫功能 病毒 Deubiquitinating enzyme Ubiquitin-specific protease 15 Tumor Immune function Virus
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  • 1Gilchrist CA, Gray DA, Baker RT. A ubiquitin-specific protease that efficiently cleaves the ubiquitin-proline bond. J Biol Chem, 1997, 272:32280-32285.
  • 2Elliott PR, Liu H, Pastok MW, et al. Structural variability of the ubiquitin specific protease DUSP-UBL double do-mains. FEBS Lett, 2011, 585:3385-3390.
  • 3Song EJ, Werner SL, Neubauer J, et al. The Prpl9 com- plex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome. Genes Dev, 2010, 24:1434-1447.
  • 4Harper S, Gratton HE, Cornaciu I, et al. Structure and catalytic regulatory function of ubiquitin specific prote- ase 11 N-terminal and ubiquitin-like domains. Biochem- istry, 2014, 53:2966-2978.
  • 5Sowa ME, Bennett E J, Gygi SP, et al. Defining the hu- man deubiquitinating enzyme interaction landscape. Cell, 2009, 138:389-403.
  • 6Hayes SD, Liu H, MacDonald E, et al. Direct and indi- rect control of mitogen-activated protein kinase path- way-associated components, BRAP/IMP E3 ubiquitin ligase and CRAF/RAF 1 kinase, by the deubiquitylating enzyme USP15. J Biol Chem, 2012, 287:43007-43018.
  • 7Frederick A, Rolfe M, Chiu MI. The human UNP locus at 3p21.31 encodes two tissue-selective, cytoplasmic isoforms with deubiquitinating activity that have reduced expression in small cell lung carcinoma cell lines. Onco- gene, 1998, 16:153-165.
  • 8Gupta K, Copeland NG, Gilbert D J, et al. Unp, a mouse gene related to the tre oncogene. Oncogene, 1993, 8: 2307-2310.
  • 9Gupta K, Chevrette M, Gray DA. The Unp proto-on- cogene encodes a nuclear protein. Oncogene, 1994, 9: 1729-1731.
  • 10Soboleva TA, Jans DA, Johnson-Saliba M, et al. Nucle- ar-cytoplasmic shuttling of the oncogenic mouse UNP/ USP4 deubiquitylating enzyme. J Biol Chem, 2005, 280: 745-752.

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